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P16615 (AT2A2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 174. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sarcoplasmic/endoplasmic reticulum calcium ATPase 2

Short name=SERCA2
Short name=SR Ca(2+)-ATPase 2
EC=3.6.3.8
Alternative name(s):
Calcium pump 2
Calcium-transporting ATPase sarcoplasmic reticulum type, slow twitch skeletal muscle isoform
Endoplasmic reticulum class 1/2 Ca(2+) ATPase
Gene names
Name:ATP2A2
Synonyms:ATP2B
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1042 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen. Isoform 2 is involved in the regulation of the contraction/relaxation cycle. Ref.19

Catalytic activity

ATP + H2O + Ca2+(Side 1) = ADP + phosphate + Ca2+(Side 2).

Enzyme regulation

Reversibly inhibited by phospholamban (PLN) at low calcium concentrations. Dephosphorylated PLN decreases the apparent affinity of the ATPase for calcium. This inhibition is regulated by the phosphorylation of PLN By similarity.

Subunit structure

Associated with phospholamban (PLN) By similarity. Isoform 1 interacts with TRAM2 (via C-terminus). Interacts with HAX1. Interacts with S100A8 and S100A9 By similarity. Ref.6 Ref.11

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein. Sarcoplasmic reticulum membrane; Multi-pass membrane protein.

Tissue specificity

Isoform 1 is widely expressed in smooth muscle and nonmuscle tissues such as in adult skin epidermis, with highest expression in liver, pancreas and lung, and intermediate expression in brain, kidney and placenta. Also expressed at lower levels in heart and skeletal muscle. Isoforms 2 and 3 are highly expressed in the heart and slow twitch skeletal muscle. Expression of isoform 3 is predominantly restricted to cardiomyocytes and in close proximity to the sarcolemma. Both isoforms are mildly expressed in lung, kidney, liver, pancreas and placenta. Expression of isoform 3 is amplified during monocytic differentiation and also observed in the fetal heart. Ref.5 Ref.15 Ref.19

Post-translational modification

Nitrated under oxidative stress. Nitration on the two tyrosine residues inhibits catalytic activity.

Involvement in disease

Acrokeratosis verruciformis (AKV) [MIM:101900]: A localized disorder of keratinization, which is inherited as an autosomal dominant trait. Its onset is early in life with multiple flat-topped, flesh-colored papules on the hands and feet, punctate keratoses on the palms and soles, with varying degrees of nail involvement. The histopathology shows a distinctive pattern of epidermal features with hyperkeratosis, hypergranulosis and acanthosis together with papillomatosis. These changes are frequently associated with circumscribed elevations of the epidermis that are said to resemble church spires. There are no features of dyskeratosis or acantholysis, the typical findings in lesions of Darier disease.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.18

Darier disease (DD) [MIM:124200]: A skin disorder characterized by warty papules and plaques in seborrheic areas (central trunk, flexures, scalp and forehead), palmoplantar pits and distinctive nail abnormalities. It is due to loss of adhesion between epidermal cells (acantholysis) and abnormal keratinization. Patients with mild disease may have no more than a few scattered keratotic papules or subtle nail changes, whereas those with severe disease are handicapped by widespread malodorous keratotic plaques. Some patients present with hemorrhage into acantholytic vesicles on the palms and dorsal aspects of the fingers which gives rise to black macules. In a few families affected by Darier disease, neuropsychiatric abnormalities such as mild mental retardation, schizophrenia, bipolar disorder and epilepsy have been reported. Stress, UV exposure, heat, sweat, friction and oral contraception exacerbate disease symptoms. Clinical variants of Darier disease include hypertrophic, vesicobullous, hypopigmented, cornifying, zosteriform or linear, acute and comedonal subtypes. Comedonal Darier disease is characterized by the coexistence of acne-like comedonal lesions with typical Darier hyperkeratotic papules on light-exposed areas. At histopathologic level, comedonal Darier disease differs from classic Darier disease in the prominent follicular involvement and the presence of greatly elongated dermal villi.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.14 Ref.15 Ref.16 Ref.17 Ref.20

Sequence similarities

Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIA subfamily. [View classification]

Sequence caution

The sequence BAG57266.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Biological processCalcium transport
Ion transport
Transport
   Cellular componentEndoplasmic reticulum
Membrane
Sarcoplasmic reticulum
   Coding sequence diversityAlternative splicing
   DiseaseDisease mutation
Epilepsy
   DomainTransmembrane
Transmembrane helix
   LigandATP-binding
Calcium
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionHydrolase
   PTMIsopeptide bond
Nitration
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processER-nucleus signaling pathway

Inferred from electronic annotation. Source: Ensembl

blood coagulation

Traceable author statement. Source: Reactome

calcium ion transmembrane transport

Traceable author statement Ref.1. Source: GOC

cell adhesion

Traceable author statement Ref.17. Source: ProtInc

cellular calcium ion homeostasis

Traceable author statement PubMed 22679139. Source: BHF-UCL

epidermis development

Traceable author statement Ref.17. Source: ProtInc

ion transmembrane transport

Traceable author statement. Source: Reactome

negative regulation of heart contraction

Inferred from electronic annotation. Source: Ensembl

positive regulation of heart rate

Traceable author statement PubMed 22679139. Source: BHF-UCL

regulation of cardiac muscle cell membrane potential

Traceable author statement PubMed 22679139. Source: BHF-UCL

regulation of the force of heart contraction

Inferred from electronic annotation. Source: Ensembl

relaxation of cardiac muscle

Traceable author statement PubMed 22679139. Source: BHF-UCL

sarcoplasmic reticulum calcium ion transport

Traceable author statement PubMed 19095005PubMed 22679139. Source: BHF-UCL

transmembrane transport

Traceable author statement. Source: Reactome

transport

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentendoplasmic reticulum membrane

Inferred from direct assay PubMed 11402072. Source: UniProtKB

integral component of plasma membrane

Traceable author statement Ref.1. Source: ProtInc

intracellular membrane-bounded organelle

Traceable author statement Ref.1. Source: ProtInc

membrane

Inferred from direct assay PubMed 22375059. Source: MGI

platelet dense tubular network membrane

Traceable author statement. Source: Reactome

sarcoplasmic reticulum

Inferred from direct assay PubMed 12804600. Source: UniProtKB

sarcoplasmic reticulum membrane

Traceable author statement PubMed 19095005. Source: BHF-UCL

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

S100 protein binding

Inferred from physical interaction PubMed 12804600. Source: UniProtKB

calcium-transporting ATPase activity

Traceable author statement Ref.1. Source: ProtInc

calcium-transporting ATPase activity involved in regulation of cardiac muscle cell membrane potential

Traceable author statement PubMed 22679139. Source: BHF-UCL

enzyme binding

Inferred from physical interaction PubMed 21903937. Source: BHF-UCL

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein C-terminus binding

Inferred from physical interaction Ref.6. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 20528919. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

OPRD1P411433EBI-358933,EBI-2624456

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Note: SERCA2 transcripts differ only in their 3'-UTR region and are expressed in a tissue-specific manner.
Isoform 1 (identifier: P16615-1)

Also known as: ATP2A2B; Class 2-4; HK1; SERCA2b;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Note: Ubiquitous housekeeping isoform.
Isoform 2 (identifier: P16615-2)

Also known as: ATP2A2A; Class 1; HK2; SERCA2a;

The sequence of this isoform differs from the canonical sequence as follows:
     994-1042: GKECVQPATKSCSFSACTDGISWPFVLLIMPLVIWVYSTDTNFSDMFWS → AILE
Note: Cardiac/slow twitch, muscle specific isoform. Has a lower affinity for calcium and a higher catalytic turnover rate.
Isoform 3 (identifier: P16615-3)

Also known as: SERCA2C;

The sequence of this isoform differs from the canonical sequence as follows:
     994-1042: GKECVQPATKSCSFSACTDGISWPFVLLIMPLVIWVYSTDTNFSDMFWS → VLSSEL
Note: May be due to intron retention. Shows a lower apparent affinity for cytosolic calcium than isoform 2 and a catalytic turnover rate similar to isoform 1.
Isoform 4 (identifier: P16615-4)

The sequence of this isoform differs from the canonical sequence as follows:
     155-181: Missing.
Note: No experimental confirmation available.
Isoform 5 (identifier: P16615-5)

The sequence of this isoform differs from the canonical sequence as follows:
     994-1042: GKECVQPATKSCSFSACTDGISWPFVLLIMPLVIWVYSTDTNFSDMFWS → DIIK
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10421042Sarcoplasmic/endoplasmic reticulum calcium ATPase 2
PRO_0000046196

Regions

Topological domain1 – 4848Cytoplasmic By similarity
Transmembrane49 – 6921Helical; Name=1; By similarity
Topological domain70 – 8920Lumenal By similarity
Transmembrane90 – 11021Helical; Name=2; By similarity
Topological domain111 – 253143Cytoplasmic By similarity
Transmembrane254 – 27320Helical; Name=3; By similarity
Topological domain274 – 29522Lumenal By similarity
Transmembrane296 – 31318Helical; Name=4; By similarity
Topological domain314 – 756443Cytoplasmic By similarity
Transmembrane757 – 77620Helical; Name=5; By similarity
Topological domain777 – 78610Lumenal By similarity
Transmembrane787 – 80721Helical; Name=6; By similarity
Topological domain808 – 82720Cytoplasmic By similarity
Transmembrane828 – 85023Helical; Name=7; By similarity
Topological domain851 – 89646Lumenal By similarity
Transmembrane897 – 91620Helical; Name=8; By similarity
Topological domain917 – 92913Cytoplasmic By similarity
Transmembrane930 – 94819Helical; Name=9; By similarity
Topological domain949 – 96315Lumenal By similarity
Transmembrane964 – 98421Helical; Name=10; By similarity
Topological domain985 – 104258Cytoplasmic By similarity
Region370 – 40031Interacts with phospholamban 1 By similarity
Region575 – 59420Interacts with HAX1
Region787 – 80721Interacts with phospholamban 2 By similarity

Sites

Active site35114-aspartylphosphate intermediate By similarity
Metal binding3041Calcium 2; via carbonyl oxygen By similarity
Metal binding3051Calcium 2; via carbonyl oxygen By similarity
Metal binding3071Calcium 2; via carbonyl oxygen By similarity
Metal binding3091Calcium 2 By similarity
Metal binding7021Magnesium By similarity
Metal binding7061Magnesium By similarity
Metal binding7671Calcium 1 By similarity
Metal binding7701Calcium 1 By similarity
Metal binding7951Calcium 2 By similarity
Metal binding7981Calcium 1 By similarity
Metal binding7991Calcium 1 By similarity
Metal binding7991Calcium 2 By similarity
Metal binding9071Calcium 1 By similarity

Amino acid modifications

Modified residue2941Nitrated tyrosine Ref.7
Modified residue2951Nitrated tyrosine Ref.7
Modified residue6631Phosphoserine Ref.8 Ref.9 Ref.12
Cross-link143Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Natural variations

Alternative sequence155 – 18127Missing in isoform 4.
VSP_039392
Alternative sequence994 – 104249GKECV…DMFWS → AILE in isoform 2.
VSP_000358
Alternative sequence994 – 104249GKECV…DMFWS → VLSSEL in isoform 3.
VSP_039393
Alternative sequence994 – 104249GKECV…DMFWS → DIIK in isoform 5.
VSP_039394
Natural variant231G → E in DD. Ref.17
Corresponds to variant rs28929478 [ dbSNP | Ensembl ].
VAR_008608
Natural variant391N → T in DD. Ref.16
VAR_008609
Natural variant411Missing in DD; comedonal type. Ref.20
VAR_063398
Natural variant471K → KMFLTGK in DD.
VAR_008610
Natural variant651L → S in DD; severe form.
VAR_008611
Natural variant1311R → Q in DD.
VAR_008612
Natural variant1601P → L in DD.
VAR_008613
Natural variant1861S → P in DD.
VAR_008614
Natural variant2111G → D in DD; severe form.
VAR_008615
Natural variant2231V → M in DD.
VAR_008616
Natural variant2681C → F in DD; haemorrhagic lesions.
VAR_008617
Natural variant3101G → V in DD.
VAR_008618
Natural variant3181C → R in DD; severe form.
VAR_008619
Natural variant3481I → T in DD.
VAR_008620
Natural variant3571T → K in DD. Ref.17
VAR_009508
Natural variant4121E → G in DD.
VAR_008621
Natural variant4951S → F in DD. Ref.17
VAR_008622
Natural variant5601C → R in DD; neuropsychiatric phenotype. Ref.16
VAR_008623
Natural variant6021P → L in AKV; loss of activity. Ref.18
VAR_017532
Natural variant6751F → S in DD; multiple neuropsychiatric features.
VAR_008624
Natural variant6831K → E in DD; depression.
VAR_008625
Natural variant7021D → N in DD; moderate form.
VAR_008626
Natural variant7451A → D in DD; moderate form.
VAR_008627
Natural variant7491G → R in DD. Ref.17
VAR_009509
Natural variant7541Missing in DD.
VAR_008628
Natural variant7651S → L in DD. Ref.16
VAR_008629
Natural variant7671N → S in DD; haemorrhagic lesions and neuropsychiatric phenotype.
VAR_008630
Natural variant7691G → R in DD.
VAR_008631
Natural variant8031A → T in DD; mild/moderate form.
VAR_008632
Natural variant8381A → P in DD; severe form; petit mal epilepsy.
VAR_008633
Natural variant8431V → F in DD; depression.
VAR_008634
Natural variant8751C → G in DD; retinitis pigmentosa.
VAR_008635
Natural variant9201S → Y in DD; mild/moderate/severe form; one patient with epilepsy.
VAR_008636
Natural variant9431H → R in DD; learning difficulties.
VAR_008637
Natural variant9751P → R in DD.
VAR_008638

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (ATP2A2B) (Class 2-4) (HK1) (SERCA2b) [UniParc].

Last modified August 1, 1990. Version 1.
Checksum: 5462FF2DA7FB630A

FASTA1,042114,757
        10         20         30         40         50         60 
MENAHTKTVE EVLGHFGVNE STGLSLEQVK KLKERWGSNE LPAEEGKTLL ELVIEQFEDL 

        70         80         90        100        110        120 
LVRILLLAAC ISFVLAWFEE GEETITAFVE PFVILLILVA NAIVGVWQER NAENAIEALK 

       130        140        150        160        170        180 
EYEPEMGKVY RQDRKSVQRI KAKDIVPGDI VEIAVGDKVP ADIRLTSIKS TTLRVDQSIL 

       190        200        210        220        230        240 
TGESVSVIKH TDPVPDPRAV NQDKKNMLFS GTNIAAGKAM GVVVATGVNT EIGKIRDEMV 

       250        260        270        280        290        300 
ATEQERTPLQ QKLDEFGEQL SKVISLICIA VWIINIGHFN DPVHGGSWIR GAIYYFKIAV 

       310        320        330        340        350        360 
ALAVAAIPEG LPAVITTCLA LGTRRMAKKN AIVRSLPSVE TLGCTSVICS DKTGTLTTNQ 

       370        380        390        400        410        420 
MSVCRMFILD RVEGDTCSLN EFTITGSTYA PIGEVHKDDK PVNCHQYDGL VELATICALC 

       430        440        450        460        470        480 
NDSALDYNEA KGVYEKVGEA TETALTCLVE KMNVFDTELK GLSKIERANA CNSVIKQLMK 

       490        500        510        520        530        540 
KEFTLEFSRD RKSMSVYCTP NKPSRTSMSK MFVKGAPEGV IDRCTHIRVG STKVPMTSGV 

       550        560        570        580        590        600 
KQKIMSVIRE WGSGSDTLRC LALATHDNPL RREEMHLEDS ANFIKYETNL TFVGCVGMLD 

       610        620        630        640        650        660 
PPRIEVASSV KLCRQAGIRV IMITGDNKGT AVAICRRIGI FGQDEDVTSK AFTGREFDEL 

       670        680        690        700        710        720 
NPSAQRDACL NARCFARVEP SHKSKIVEFL QSFDEITAMT GDGVNDAPAL KKAEIGIAMG 

       730        740        750        760        770        780 
SGTAVAKTAS EMVLADDNFS TIVAAVEEGR AIYNNMKQFI RYLISSNVGE VVCIFLTAAL 

       790        800        810        820        830        840 
GFPEALIPVQ LLWVNLVTDG LPATALGFNP PDLDIMNKPP RNPKEPLISG WLFFRYLAIG 

       850        860        870        880        890        900 
CYVGAATVGA AAWWFIAADG GPRVSFYQLS HFLQCKEDNP DFEGVDCAIF ESPYPMTMAL 

       910        920        930        940        950        960 
SVLVTIEMCN ALNSLSENQS LLRMPPWENI WLVGSICLSM SLHFLILYVE PLPLIFQITP 

       970        980        990       1000       1010       1020 
LNVTQWLMVL KISLPVILMD ETLKFVARNY LEPGKECVQP ATKSCSFSAC TDGISWPFVL 

      1030       1040 
LIMPLVIWVY STDTNFSDMF WS 

« Hide

Isoform 2 (ATP2A2A) (Class 1) (HK2) (SERCA2a) [UniParc].

Checksum: DD57D12A2B24FEC1
Show »

FASTA997109,691
Isoform 3 (SERCA2C) [UniParc].

Checksum: F6BE03E546453B24
Show »

FASTA999109,893
Isoform 4 [UniParc].

Checksum: 6C99B5C382834A63
Show »

FASTA1,015111,847
Isoform 5 [UniParc].

Checksum: D570A12D5B24FEC1
Show »

FASTA997109,734

References

« Hide 'large scale' references
[1]"Molecular cloning of cDNAs from human kidney coding for two alternatively spliced products of the cardiac Ca2+-ATPase gene."
Lytton J., Maclennan D.H.
J. Biol. Chem. 263:15024-15031(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2).
Tissue: Kidney.
[2]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Eye.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 84-1042 (ISOFORM 4).
Tissue: Cerebellum.
[5]"Identification of a new SERCA2 splice variant regulated during monocytic differentiation."
Gelebart P., Martin V., Enouf J., Papp B.
Biochem. Biophys. Res. Commun. 303:676-684(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 954-1042 (ISOFORM 3), TISSUE SPECIFICITY.
[6]"TRAM2 protein interacts with endoplasmic reticulum Ca2+ pump Serca2b and is necessary for collagen type I synthesis."
Stefanovic B., Stefanovic L., Schnabl B., Bataller R., Brenner D.A.
Mol. Cell. Biol. 24:1758-1768(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TRAM2.
[7]"Detection of sequence-specific tyrosine nitration of manganese SOD and SERCA in cardiovascular disease and aging."
Xu S., Ying J., Jiang B., Guo W., Adachi T., Sharov V., Lazar H., Menzoian J., Knyushko T.V., Bigelow D., Schoeneich C., Cohen R.A.
Am. J. Physiol. 290:H2220-H2227(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NITRATION AT TYR-294 AND TYR-295.
[8]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-663, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-663, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"The anti-apoptotic protein HAX-1 interacts with SERCA2 and regulates its protein levels to promote cell survival."
Vafiadaki E., Arvanitis D.A., Pagakis S.N., Papalouka V., Sanoudou D., Kontrogianni-Konstantopoulos A., Kranias E.G.
Mol. Biol. Cell 20:306-318(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HAX1.
[12]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-663, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[13]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Spectrum of novel ATP2A2 mutations in patients with Darier's disease."
Sakuntabhai A., Burge S., Monk S., Hovnanian A.
Hum. Mol. Genet. 8:1611-1619(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS DD.
[15]"ATP2A2 mutations in Darier's disease: variant cutaneous phenotypes are associated with missense mutations, but neuropsychiatric features are independent of mutation class."
Ruiz-Perez V.L., Carter S.A., Healy E., Todd C., Rees J.L., Steijlen P.M., Carmichael A.J., Lewis H.M., Hohl D., Itin P., Vahlquist A., Gobello T., Mazzanti C., Reggazini R., Nagy G., Munro C.S., Strachan T.
Hum. Mol. Genet. 8:1621-1630(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS DD, TISSUE SPECIFICITY.
[16]"ATP2A2 mutations in Darier's disease and their relationship to neuropsychiatric phenotypes."
Jacobsen N.J.O., Lyons I., Hoogendoorn B., Burge S., Kwok P.-Y., O'Donovan M.C., Craddock N., Owen M.J.
Hum. Mol. Genet. 8:1631-1636(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS DD THR-39; ARG-560 AND LEU-765.
[17]"Mutations in ATP2A2, encoding a Ca2+ pump, cause Darier disease."
Sakuntabhai A., Ruiz-Perez V., Carter S., Jacobsen N., Burge S., Monk S., Smith M., Munro C.S., O'Donovan M.C., Craddock N., Kucherlapati R., Rees J.L., Owen M.J., Lathrop G.M., Monaco A.P., Strachan T., Hovnanian A.
Nat. Genet. 21:271-277(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS DD GLU-23; LYS-357; PHE-495 AND ARG-749.
[18]"Acrokeratosis verruciformis of Hopf is caused by mutation in ATP2A2: evidence that it is allelic to Darier's disease."
Dhitavat J., Macfarlane S., Dode L., Leslie N., Sakuntabhai A., MacSween R., Saihan E., Hovnanian A.
J. Invest. Dermatol. 120:229-232(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AKV LEU-602.
[19]"Ca2+-ATPases in non-failing and failing heart: evidence for a novel cardiac sarco/endoplasmic reticulum Ca2+-ATPase 2 isoform (SERCA2c)."
Dally S., Bredoux R., Corvazier E., Andersen J.P., Clausen J.D., Dode L., Fanchaouy M., Gelebart P., Monceau V., Del Monte F., Gwathmey J.K., Hajjar R., Chaabane C., Bobe R., Raies A., Enouf J.
Biochem. J. 395:249-258(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[20]"Three-base deletion mutation c.120_122delGTT in ATP2A2 leads to the unique phenotype of comedonal Darier disease."
Tsuruta D., Akiyama M., Ishida-Yamamoto A., Imanishi H., Mizuno N., Sowa J., Kobayashi H., Ishii M., Kurokawa I., Shimizu H.
Br. J. Dermatol. 162:687-689(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT DD LEU-41 DEL.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M23114 mRNA. Translation: AAA53193.1.
M23116 Genomic DNA. Translation: AAA52757.1.
M23115 mRNA. Translation: AAA53194.1.
M23278, M23116 Genomic DNA. Translation: AAA52758.1.
AC006088 Genomic DNA. No translation available.
BC035588 mRNA. Translation: AAH35588.1.
AK293877 mRNA. Translation: BAG57266.1. Different initiation.
AY186578 mRNA. Translation: AAO47398.1.
CCDSCCDS9143.1. [P16615-2]
CCDS9144.1. [P16615-1]
PIRA31981.
B31981.
RefSeqNP_001672.1. NM_001681.3. [P16615-2]
NP_733765.1. NM_170665.3. [P16615-1]
XP_005253945.1. XM_005253888.1. [P16615-3]
UniGeneHs.506759.

3D structure databases

ProteinModelPortalP16615.
SMRP16615. Positions 1-992.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106978. 46 interactions.
IntActP16615. 16 interactions.
MINTMINT-4991144.
STRING9606.ENSP00000324892.

Chemistry

BindingDBP16615.
ChEMBLCHEMBL3901.

Protein family/group databases

TCDB3.A.3.2.7. the p-type atpase (p-atpase) superfamily.

PTM databases

PhosphoSiteP16615.

Polymorphism databases

DMDM114312.

Proteomic databases

MaxQBP16615.
PaxDbP16615.
PRIDEP16615.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000308664; ENSP00000311186; ENSG00000174437. [P16615-2]
ENST00000395494; ENSP00000378872; ENSG00000174437. [P16615-4]
ENST00000539276; ENSP00000440045; ENSG00000174437. [P16615-1]
ENST00000553144; ENSP00000450407; ENSG00000174437.
GeneID488.
KEGGhsa:488.
UCSCuc001tqk.4. human. [P16615-1]
uc001tql.4. human. [P16615-2]

Organism-specific databases

CTD488.
GeneCardsGC12P110719.
HGNCHGNC:812. ATP2A2.
HPAHPA062605.
MIM101900. phenotype.
108740. gene.
124200. phenotype.
neXtProtNX_P16615.
Orphanet79151. Acrokeratosis verruciformis of Hopf.
218. Darier disease.
PharmGKBPA71.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0474.
HOGENOMHOG000265621.
HOVERGENHBG105648.
InParanoidP16615.
KOK05853.
OMARVEGDTC.
OrthoDBEOG73Z2SF.
PhylomeDBP16615.
TreeFamTF300651.

Enzyme and pathway databases

ReactomeREACT_15518. Transmembrane transport of small molecules.
REACT_604. Hemostasis.
SignaLinkP16615.

Gene expression databases

ArrayExpressP16615.
BgeeP16615.
CleanExHS_ATP2A2.
GenevestigatorP16615.

Family and domain databases

Gene3D1.20.1110.10. 2 hits.
2.70.150.10. 2 hits.
3.40.1110.10. 1 hit.
InterProIPR005782. ATPase_P-typ_Ca-transp_IIA.
IPR006068. ATPase_P-typ_cation-transptr_C.
IPR004014. ATPase_P-typ_cation-transptr_N.
IPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR023298. ATPase_P-typ_TM_dom.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR001757. Cation_transp_P_typ_ATPase.
IPR023214. HAD-like_dom.
[Graphical view]
PfamPF00689. Cation_ATPase_C. 1 hit.
PF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
PF00702. Hydrolase. 1 hit.
[Graphical view]
PRINTSPR00119. CATATPASE.
PR00120. HATPASE.
SMARTSM00831. Cation_ATPase_N. 1 hit.
[Graphical view]
SUPFAMSSF56784. SSF56784. 1 hit.
SSF81660. SSF81660. 1 hit.
TIGRFAMsTIGR01116. ATPase-IIA1_Ca. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.
PROSITEPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSATP2A2. human.
GenomeRNAi488.
NextBio2031.
PROP16615.
SOURCESearch...

Entry information

Entry nameAT2A2_HUMAN
AccessionPrimary (citable) accession number: P16615
Secondary accession number(s): A6NDN7 expand/collapse secondary AC list , B4DF05, P16614, Q86VJ2
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: July 9, 2014
This is version 174 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM